Lineage for d2tpra1 (2tpr A:1-168,A:286-357)

  1. Root: SCOPe 2.06
  2. 2078559Class c: Alpha and beta proteins (a/b) [51349] (148 folds)
  3. 2096453Fold c.3: FAD/NAD(P)-binding domain [51904] (1 superfamily)
    core: 3 layers, b/b/a; central parallel beta-sheet of 5 strands, order 32145; top antiparallel beta-sheet of 3 strands, meander
  4. 2096454Superfamily c.3.1: FAD/NAD(P)-binding domain [51905] (9 families) (S)
  5. 2096984Family c.3.1.5: FAD/NAD-linked reductases, N-terminal and central domains [51943] (15 protein domains)
    duplication: both domains have similar folds and functions
    most members of the family contain common C-terminal alpha+beta domain
  6. 2097273Protein Trypanothione reductase [51947] (3 species)
  7. 2097274Species Crithidia fasciculata [TaxId:5656] [51948] (6 PDB entries)
  8. 2097291Domain d2tpra1: 2tpr A:1-168,A:286-357 [30505]
    Other proteins in same PDB: d2tpra3, d2tprb3
    complexed with fad

Details for d2tpra1

PDB Entry: 2tpr (more details), 2.4 Å

PDB Description: x-ray structure of trypanothione reductase from crithidia fasciculata at 2.4 angstroms resolution
PDB Compounds: (A:) trypanothione reductase

SCOPe Domain Sequences for d2tpra1:

Sequence; same for both SEQRES and ATOM records: (download)

>d2tpra1 c.3.1.5 (A:1-168,A:286-357) Trypanothione reductase {Crithidia fasciculata [TaxId: 5656]}

SCOPe Domain Coordinates for d2tpra1:

Click to download the PDB-style file with coordinates for d2tpra1.
(The format of our PDB-style files is described here.)

Timeline for d2tpra1: